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   <subfield code="a">Activity, stability and kinetic parameters for α -chymotrypsin catalysed reactions in AOT/isooctane reverse micelles with nonionic and zwitterionic mixed surfactants</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[SANTOSH VERMA, KALLOL GHOSH]</subfield>
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   <subfield code="a">Reverse micelles (RMs) of sodium 1,4-bis(2-ethylhexyl)sulphosuccinate (AOT) in nonpolar organic solvents are widely known to have very high solubilization power for water. The method is applied to the hydrolysis of p-nitrophenyl acetate (PNPA) catalysed by α-chymotrypsin (α-CT) in AOT/isooctane/buffer RMs. The increase in α-CT activity and stability was an optimum at w o ([H2O]/[AOT]) = 10, z [Isooctane]/[AOT]) = 5. Three typical surfactants were selected based on their head group charges: a non-ionic surfactant Triton-X 100 and two zwitterionic sulphobetaine surfactants of the type C n H2n + 1N + Me2 (CH $_{2})_{3\thinspace }$ SO $_{3}^{-}$ (n = 10; SB3-10, n = 16; SB3-16). The kinetic parameters (such as k cat and K M) of the α-CT at 27°C were determined and compared in the absence and presence of three surfactants. The effect of chain length of zwitterionic surfactant (SB3-10 and SB3-16) on the enzymatic efficacy of α-CT as a function of mixed surfactant addition has been investigated in AOT/isooctane RMs at pH 7.75. Graphical Abstract The α-chymotrypsin (α-CT) hydrolysis of p-nitrophenyl acetate (PNPA) in AOT/isooctane/buffer reverse micelles (RMs) have been studied with varying water content, wo, in the presence of Triton-X 100 and sulphobetaine surfactants. The activity of α-CT depends on the water pool size and the amount of AOT and mixed surfactant media.</subfield>
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   <subfield code="a">Indian Academy of Sciences, 2013</subfield>
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